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X-ray scattering experiments with high-flux X-ray source coupled rapid mixing microchannel device and their potential for high-flux neutron scattering investigations.

MPS-Authors
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Jain,  R.
Research Group of Structural Dynamics of (Bio)Chemical Systems, MPI for biophysical chemistry, Max Planck Society;

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Petri,  M.
Research Group of Structural Dynamics of (Bio)Chemical Systems, MPI for biophysical chemistry, Max Planck Society;

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Kirschbaum,  S.
Research Group of Biological Micro- and Nanotechnology, MPI for biophysical chemistry, Max Planck Society;

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Sonnenkalb,  S.
Research Group of Structural Dynamics of (Bio)Chemical Systems, MPI for biophysical chemistry, Max Planck Society;

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Becker,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Griesinger,  C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Burg,  T. P.
Research Group of Biological Micro- and Nanotechnology, MPI for biophysical chemistry, Max Planck Society;

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Techert,  S.
Research Group of Structural Dynamics of (Bio)Chemical Systems, MPI for biophysical chemistry, Max Planck Society;

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Citation

Jain, R., Petri, M., Kirschbaum, S., Feindt, H., Steltenkamp, S., Sonnenkalb, S., et al. (2013). X-ray scattering experiments with high-flux X-ray source coupled rapid mixing microchannel device and their potential for high-flux neutron scattering investigations. The European Physical Journal E, 36(9): 109. doi:10.1140/epje/i2013-13109-9.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0014-7A8F-7
Abstract
Small-angle X-ray scattering provides global, shape-sensitive structural information about macromolecules in solution. Its extension to time dimension in the form of time-resolved SAXS investigations and combination with other time-resolved biophysical methods contributes immensely to the study of protein dynamics. TR-SAXS can also provide unique information about the global structures of transient intermediates during protein dynamics. An experimental set-up with low protein consumption is essential for an extensive use of TR-SAXS experiments on protein dynamics. In this direction, a newly developed 20-microchannel microfluidic continuous-flow mixer was combined with SAXS. With this set-up, we demonstrate ubiquitin unfolding dynamics after rapid mixing with the chaotropic agent Guanidinium-HCl within milliseconds using only 40 nanoliters of the protein sample per scattering image. It is suggested that, in the future, this new TR-SAXS platform will help to increase the use of time-resolved small-angle X-ray scattering, wide-angle X-ray scattering and neutron scattering experiments for studying protein dynamics in the early millisecond regime. The potential research field for this set-up includes protein folding, protein misfolding, aggregation in amyloidogenic diseases, function of intrinsically disordered proteins and various protein-ligand interactions.